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• W2008451770 endingPage "91" @default.
• W2008451770 startingPage "76" @default.
• W2008451770 abstract "Adaptation of microorganisms to changing osmotic conditions is a prerequisite for survival and cellular vitality for most microorganisms. In the Gram-positive soil bacterium <i>Bacillus subtilis</i>, five transport systems catalyze the uptake of compatible solutes across the plasma membrane that allow the growth of <i>B. subtilis </i>over a wide range of osmotic conditions. Focus of this review is the osmoprotectant uptake A (OpuA) transporter, a member of the family of substrate-binding protein (SBP)-dependent ATP-binding cassette (ABC) transporters that mediates the uptake of the compatible solutes glycine betaine and proline betaine. OpuA is composed of three subunits: a nucleotide-binding domain (OpuAA) located in the cytosol, a transmembrane domain (OpuAB), and a SBP (OpuAC), which binds glycine betaine and proline betaine with high specificity and targets it to OpuAB for ATP-dependent translocation across the plasma membrane. After a brief introduction in the field of bacterial osmoadaptation, we will summarize our recent findings about the biochemical and structural analysis of the components of the OpuA systems. Our studies covered both the isolated subunits of the OpuA transporter and initial investigations of the whole transporter in vitro." @default.
• W2008451770 created "2016-06-24" @default.
• W2008451770 creator A5046618148 @default.
• W2008451770 creator A5047392065 @default.
• W2008451770 creator A5061077016 @default.
• W2008451770 creator A5064520474 @default.
• W2008451770 creator A5071515962 @default.
• W2008451770 date "2005-01-01" @default.
• W2008451770 modified "2023-10-14" @default.
• W2008451770 title "Biochemical and Structural Analysis of the <i>Bacillus subtilis </i>ABC Transporter OpuA and Its Isolated Subunits" @default.
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